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Journal of Lipid Research, Vol 37, 773-782, Copyright © 1996 by Lipid Research, Inc.
JA Hamilton, JM Vural, YA Carpentier and RJ Deckelbaum
The ability of water-insoluble molecules such as triacylglycerols to
partition from oil phases into phospholipid interfaces may be crucial to
their hydrolysis by lipases in the aqueous environment of plasma and cells.
This study uses high resolution and magic angle spinning 13C NMR
spectros-copy to measure the solubility of the 8-carbon medium chain
triacylglycerol, trioctanoin, in the lamellar structure of phospholipids
(vesicles and multilayers) in the presence of other neutral lipids that may
compete for an interfacial location (long chain triacylglycerol,
cholesteryl ester, and cholesterol). In the presence of a saturating
concentration of triolein (approximately 3 mole%), the solubility of
trioctanoin in egg phosphatidylcholine vesicles decreased from 10 mole% to
7 mole%. The presence of a saturating concentration of trioctanoin
(approximately 10 mole%) decreased the interfacial solubility of long chain
triolein to approximately 1 mole%. Cholesteryl oleate in phospholipid
vesicles slightly diminished the incorporation of trioctanoin into the
surface. The presence of cholesterol reduced the interfacial solubility of
trioctanoin, but at a high level of cholesterol (30 mole%), trioctanoin had
a solubility of 3 mole%. Thus, even in the presence of other competing
neutral lipids, medium chain triacylglycerol retains a favorable location
and surface concentration for efficient hydrolysis. 13C NMR analysis thus
provides an explanation for preferential hydrolysis of medium, compared to
long chain triacylglycerol, in a physical blend of medium and long chain
triacylglycerol in a single emulsion particle, and in general, a valuable
approach to determine substrate availability at phospholipid surfaces.
ARTICLES
Incorporation of medium chain triacylglycerols into phospholipid bilayers: effect of long chain triacylglycerols, cholesterol, and cholesteryl esters
Department of Biophysics, Boston University School of Medicine, MA 02118-2394, USA.
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